Functional intermediate in the refolding pathway of a large and multidomain protein malate synthase G

Biochemistry

Volumn 52, Issue 26, 2013, Pages 4517-4530

  Dahiya, Vinay ^a   Chaudhuri, Tapan K ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE INTERMEDIATES; ENZYMATIC ACTIVITIES; INTRINSIC TRYPTOPHAN FLUORESCENCES; MULTIDOMAIN PROTEINS; PROLINE ISOMERIZATION; PROTEIN CONCENTRATIONS; REFOLDING PATHWAYS; TRYPTOPHAN FLUORESCENCE;

AMINO ACIDS; FLUORESCENCE; FLUOROPHORES;

PROTEINS;

MALATE SYNTHASE; PROTEIN MALATE SYNTHASE G; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; BIOLOGY; ENZYME ACTIVITY; EXPRESSION VECTOR; GEL PERMEATION CHROMATOGRAPHY; GENE SEQUENCE; IN VITRO STUDY; ISOMERIZATION; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN REFOLDING; UNFOLDED PROTEIN RESPONSE;

CIRCULAR DICHROISM; CLONING, MOLECULAR; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FLUORESCENCE; KINETICS; MALATE SYNTHASE; PROLINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

EID: 84880148326     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400328a     Document Type: Article

References (36)

1. Jamin, M. and Baldwin, R. L. (1996) Refolding and unfolding kinetics of the equilibrium unfolding intermediate of apomyoglobin Nature 3, 613-619
2. Chaudhuri, T. K., Arai, M., Terada, T. P., Ikura, T., and Kuwajima, K. (2000) Equilibriums and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy Biochemistry 39, 15643-15651
3. Baryshnikova, E. N., Melnik, B. S., Finkelsteinx, A. V., Semisotnov, G. V., and Bychkova, V. E. (2005) Three-state protein folding: experimental determination of free energy profile Protein Sci. 14, 2658-2667
4. Arai, M. and Kuwajima, K. (1996) Rapid formation of a molten globule intermediate in refolding of α lactalbumin Folding Des. 1, 275-285
5. Matthews, B. W. (1993) Structural and genetic analysis of protein stability Annu. Rev. Biochem. 62, 139-160
6. Schindler, T., Herder, M., Marahiel, M. A., and Schmid, F. X. (1995) Extremely rapid protein folding in the absence of intermediates Nat. Struct. Biol. 2, 663-673
7. Teilum, K., Maki, K., Kragelund, B. B., Poulsen, F. M., and Roder, H. (2002) Early kinetic intermediate in the folding of Acyl-Coenzyme A binding protein detected by fluorescence labeling and ultra rapid mixing Proc. Natl. Acad. Sci. U. S. A. 99, 9807-9812
8. Orengo, C. A. and Thornton, J. M. (2005) Protein families and their evolution-a structural perspective Annu. Rev. Biochem. 74, 867-900
9. Houry, W. A., Frishman, D., Eckerskorn, C., Lottspeich, F., and Hartl, F. U. (1999) Identification of in vivo substrates of the chaperonin GroEL Nature 402, 147-154
10. Frydman, J. (2001) Folding of newly translated proteins in vivo: The role of molecular chaperones Annu. Rev. Biochem. 70, 603-647
11. Molina, I., Pellicer, M., Badia, J., Aguilar, J., and Baldoma, L. (1994) Molecular characterization of Escherichia coli malate synthase G. Differentiation with the malate synthase A isoenzyme Eur. J. Biochem. 224, 541-548
12. Berg, J. M., Tymoczko, J. L., and Stryer, L. (2002) The citric acid cycle, in Biochemistry, 5th ed., p 484, WH Freeman & Co., New York.
13. Howard, B. R., Endrizzi, J. A., and Remington, S. J. (2000) Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 Å resolution: mechanistic implications Biochemistry 39, 3156-3168
14. Tugarinov, V., Choy, W. Y., Orekhov, V. Y., and Kay, L. E. (2005) Solution NMR-derived global fold of a monomeric 82-kDa enzyme Proc. Natl. Acad. Sci. U. S. A. 102, 622-627
15. Privalov, P. L. and Khechinashvilli, N. N. (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study J. Mol. Biol. 86, 665-684
16. Privalov, P. L. (1982) Stability of proteins: proteins which do not present a single co-operative system Adv. Protein Chem. 35, 1-104
17. Ramsay, G. and Freire, E. (1990) Linked thermal and solute perturbation analysis of co-operative domain interactions in proteins. Structural stability of diphtheria toxin Biochemistry 29, 8677-8683
18. Han, J. H., Batey, S., Nickson, A. A., Teichmann, S. A., and Clarke, J. (2007) The folding and evolution of multi-domain proteins Nat. Rev. Mol. Cell Biol. 8, 319-330
19. Privalov, P. L. (1996) Intermediate states in protein folding J. Mol. Biol. 258, 707-725
20. Sudharshan, E. and Rao, A. G. (1999) Involvement of cysteine residues and domain interactions in the reversible unfolding of lipoxygenase-I J. Biol. Chem. 274, 35351-35358
21. Lilie, H., Schwarz, E., and Rudolph, R. (1998) Advances in refolding of proteins produced in E. coli Curr. Opin. Biotechnol. 9, 497-501
22. Gardner, K. H., Zhang, X., Gehring, K., and Kay, L. E. (1998) Solution NMR studies of a 42 kDa Escherichia coli maltose binding protein/β- cyclodextrin complex: chemical shift assignments and analysis J. Am. Chem. Soc. 120, 11738-11748
23. Zettlmeissl, G., Rudolph, R., and Jaenicke, R. (1979) Reconstitution of lactic dehydrogenase noncovalent aggregation vs reactivation: physical properties and kinetics of aggregation Biochemistry 18, 5567-5571
24. Duy, C. and Fitter, J. (2006) How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra Biophys. J. 90, 3704-3711
25. Tanford, C. (1968) Protein denaturation Adv. Protein Chem. 23, 121-282
26. Buchner, J. and Kiefhaber, T. (2005) Protein Folding Handbook, Vol. 1-5, Wiley-VCH Verlag, Weinheim, Germany.
27. Stryer, L. (1965) The interaction of naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites J. Mol. Biol. 13, 482-495
28. Yang, J. T., Wu, C. S., and Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism Methods Enzymol. 130, 208-269
29. Shastry, M. C. and Udgaonkar, J. B. (1995) The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates J. Mol. Biol. 247, 1013-1027
30. Park, S. H., Shastry, M. C., and Roder, H. (1999) Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing Nat. Struct. Biol. 6, 943-947
31. Juneja, J. and Udgaonkar, J. B. (2002) Characterization of the unfolding of ribonuclease A by a pulsed hydrogen exchange study: evidence for competing pathways for unfolding Biochemistry 41, 2641-2654
32. Nall, B. T. (1994) Proline isomerisation as a rate-limiting step. Mechanisms of Protein Folding (Pain, R. H., Ed.) pp 80-103, IRL Press at Oxford University Press, Oxford, UK.
33. Khan, F., Chuang, J. I., Gianni, S., and Fersht, A. R. (2003) The kinetic pathway of folding of barnase J. Mol. Biol. 333, 169-186
34. Vendruscolo, M., Paci, E., Karplus, M., and Dobson, C. M. (2003) Structures and relative free energies of partially folded states of proteins Proc. Natl. Acad. Sci. U. S. A. 100, 14817-14821
35. Fink, A. L. (1995) Compact intermediate states in protein folding Annu. Rev. Biophys. Biomol. Struct. 24, 495-522
36. Arai, M., Ikura, T., Semisotnov, G. V., Kihara, H., Amemiya, Y., and Kuwajima, K. (1998) Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy J. Mol. Biol. 275, 149-162